DHML_PARVE
ID DHML_PARVE Reviewed; 188 AA.
AC P22641; Q56458;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Methylamine dehydrogenase light chain;
DE Short=MADH;
DE EC=1.4.9.1;
DE AltName: Full=Methylamine dehydrogenase (amicyanin);
DE AltName: Full=Methylamine dehydrogenase subunit beta;
DE Flags: Precursor;
GN Name=mauA; Synonyms=madB;
OS Paracoccus versutus (Thiobacillus versutus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=34007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1765062; DOI=10.1111/j.1432-1033.1991.tb16462.x;
RA Ubbink M., van Kleef M.A., Kleinjan D.J., Hoitink C.W., Huitema F.,
RA Beintema J.J., Duine J.A., Canters G.W.;
RT "Cloning, sequencing and expression studies of the genes encoding amicyanin
RT and the beta-subunit of methylamine dehydrogenase from Thiobacillus
RT versutus.";
RL Eur. J. Biochem. 202:1003-1012(1991).
RN [2]
RP PROTEIN SEQUENCE OF 58-188, AND X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX PubMed=2792083; DOI=10.1002/j.1460-2075.1989.tb08339.x;
RA Vellieux F.M.D., Huitema F., Groendijk H., Kalk K.H., Jzn J.F.,
RA Jongejan J.A., Duine J.A., Petratos K., Drenth J., Hol W.G.J.;
RT "Structure of quinoprotein methylamine dehydrogenase at 2.25-A
RT resolution.";
RL EMBO J. 8:2171-2178(1989).
RN [3]
RP PROTEIN SEQUENCE OF 58-66.
RX PubMed=7901050; DOI=10.1016/0014-5793(93)80402-g;
RA Van Beeumen J., Van Driessche G., Huitema F., Duine J.A., Canters G.W.;
RT "N-terminal heterogeneity of methylamine dehydrogenase from Thiobacillus
RT versutus.";
RL FEBS Lett. 333:188-192(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX PubMed=2085423; DOI=10.1107/s010876819000636x;
RA Vellieux F.M.D., Kalk K.H., Hol W.G.J.;
RT "Structure determination of quinoprotein methylamine dehydrogenase from
RT Thiobacillus versutus.";
RL Acta Crystallogr. B 46:806-823(1990).
CC -!- FUNCTION: Methylamine dehydrogenase carries out the oxidation of
CC methylamine. Electrons are passed from methylamine dehydrogenase to
CC amicyanin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methylamine + 2 oxidized [amicyanin] = formaldehyde + 2
CC H(+) + NH4(+) + 2 reduced [amicyanin]; Xref=Rhea:RHEA:30207,
CC Rhea:RHEA-COMP:11100, Rhea:RHEA-COMP:11101, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16842, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29036, ChEBI:CHEBI:49552, ChEBI:CHEBI:59338; EC=1.4.9.1;
CC -!- COFACTOR:
CC Name=tryptophan tryptophylquinone residue; Xref=ChEBI:CHEBI:20251;
CC Note=Uses a protein-derived tryptophan tryptophylquinone (TTQ)
CC cofactor.;
CC -!- PATHWAY: One-carbon metabolism; methylamine degradation; formaldehyde
CC from methylamine: step 1/1.
CC -!- SUBUNIT: Heterotetramer of two light and two heavy chains.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- PTM: Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the
CC indole ring of a tryptophan to form tryptophylquinone followed by
CC covalent cross-linking with another tryptophan residue.
CC -!- SIMILARITY: Belongs to the aromatic amine dehydrogenase light chain
CC family. {ECO:0000305}.
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DR EMBL; M58001; AAA50570.1; -; Genomic_DNA.
DR PIR; S19731; S19731.
DR RefSeq; WP_036750427.1; NZ_QUMX01000042.1.
DR PDB; 1MAE; X-ray; 2.80 A; L=64-187.
DR PDB; 1MAF; X-ray; 2.60 A; L=64-187.
DR PDB; 2MAD; X-ray; 2.25 A; L=64-187.
DR PDB; 3C75; X-ray; 2.50 A; L/M=1-188.
DR PDBsum; 1MAE; -.
DR PDBsum; 1MAF; -.
DR PDBsum; 2MAD; -.
DR PDBsum; 3C75; -.
DR AlphaFoldDB; P22641; -.
DR SMR; P22641; -.
DR STRING; 34007.IT40_03120; -.
DR eggNOG; ENOG502ZHBX; Bacteria.
DR OrthoDB; 1619371at2; -.
DR BioCyc; MetaCyc:MON-3902; -.
DR UniPathway; UPA00895; UER00870.
DR EvolutionaryTrace; P22641; -.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0030058; F:amine dehydrogenase activity; IEA:InterPro.
DR GO; GO:0052876; F:methylamine dehydrogenase (amicyanin) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
DR Gene3D; 2.60.30.10; -; 1.
DR InterPro; IPR016008; Amine_DH_Ltc.
DR InterPro; IPR036560; MADH/AADH_L_sf.
DR InterPro; IPR013504; MADH/AADH_Ltc_C_dom.
DR InterPro; IPR004229; MeN_DH_Ltc.
DR Pfam; PF02975; Me-amine-dh_L; 1.
DR PIRSF; PIRSF000192; Amine_dh_beta; 1.
DR SUPFAM; SSF57561; SSF57561; 1.
DR TIGRFAMs; TIGR02659; TTQ_MADH_Lt; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Oxidoreductase; Periplasm; Signal; Transport; TTQ.
FT SIGNAL 1..57
FT /note="Tat-type signal"
FT /evidence="ECO:0000269|PubMed:2792083,
FT ECO:0000269|PubMed:7901050"
FT CHAIN 58..188
FT /note="Methylamine dehydrogenase light chain"
FT /id="PRO_0000025576"
FT MOD_RES 114
FT /note="Tryptophylquinone"
FT DISULFID 80..145
FT DISULFID 86..118
FT DISULFID 93..178
FT DISULFID 95..143
FT DISULFID 103..134
FT DISULFID 135..166
FT CROSSLNK 114..165
FT /note="Tryptophan tryptophylquinone (Trp-Trp)"
FT CONFLICT 89
FT /note="D -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="G -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="N -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..112
FT /note="KLATA -> LVASG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..129
FT /note="TDGQSYLI -> PDPNKYIT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="P -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..159
FT /note="RPEF -> NKD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="A -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 172..173
FT /note="DA -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 183..188
FT /note="IVGKAS -> VSGA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2MAD"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2MAD"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2MAD"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2MAD"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2MAD"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:2MAD"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:2MAD"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:2MAD"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2MAD"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2MAD"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2MAD"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2MAD"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2MAD"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2MAD"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2MAD"
SQ SEQUENCE 188 AA; 20358 MW; 923C5461737C63FA CRC64;
MLGNFRFDDM VEKLSRRVAG RTSRRGAIGR LGTVLAGAAL VPLLPVDRRG RVSRANAAGP
AEGVDPRAKW QPQDNDIQAC DYWRHCSIDG NICDCSGGSL TNCPPGTKLA TASWVASCYN
PTDGQSYLIA YRDCCGYNVS GRCPCLNTEG ELPVYRPEFA NDIIWCFGAE DDAMTYHCTI
SPIVGKAS
